Evidence map›Paper›PMID 30154480›Full record

ArticleNature communications2018

AXER is an ATP/ADP exchanger in the membrane of the endoplasmic reticulum.

Marie-Christine Klein, Katharina Zimmermann, Stefan Schorr, Martina Landini, Patrick A W Klemens, Jacqueline Altensell, Martin Jung, Elmar Krause, Duy Nguyen, Volkhard Helms and 9 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
4.4field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

42 citing papers in PubMed, 67 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. The oncogene SLC35F2 is a high-specificity transporter for the micronutrients queuine and queuosine.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Editorial: The evolving picture of CaFrontiers in physiology · 2023
    Article
  12. Kinetics of the thapsigargin-induced CaFrontiers in physiology · 2023
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

19 authors at 3 institutions in 1 country.

Marie-Christine KleinMedical Biochemistry and Molecular Biology, Saarland University, 66421, Homburg, Germany.
Katharina ZimmermannBiophysics, CIPMM Saarland University, 66421, Homburg, Germany.
Stefan SchorrMedical Biochemistry and Molecular Biology, Saarland University, 66421, Homburg, Germany.
Martina LandiniPlant Physiology, Technical University Kaiserslautern, 67663, Kaiserslautern, Germany.
Patrick A W KlemensPlant Physiology, Technical University Kaiserslautern, 67663, Kaiserslautern, Germany.
Jacqueline AltensellPlant Physiology, Technical University Kaiserslautern, 67663, Kaiserslautern, Germany.
Martin JungMedical Biochemistry and Molecular Biology, Saarland University, 66421, Homburg, Germany.ORCID http://orcid.org/0000-0002-1482-7020
Elmar KrausePhysiology, CIPMM Saarland University, 66421, Homburg, Germany.
Duy NguyenCenter for Bioinformatics, Saarland University, 66041, Saarbrücken, Germany.
Volkhard HelmsCenter for Bioinformatics, Saarland University, 66041, Saarbrücken, Germany.ORCID http://orcid.org/0000-0002-2180-9154
Jens RettigPhysiology, CIPMM Saarland University, 66421, Homburg, Germany.
Claudia Fecher-TrostExperimental and Clinical Pharmacology and Toxicology, Saarland University, 66421, Homburg, Germany.
Adolfo CavaliéExperimental and Clinical Pharmacology and Toxicology, Saarland University, 66421, Homburg, Germany.
Markus HothBiophysics, CIPMM Saarland University, 66421, Homburg, Germany.ORCID http://orcid.org/0000-0001-7080-4643
Ivan BogeskiBiophysics, CIPMM Saarland University, 66421, Homburg, Germany. ivan.bogeski@med.uni-goettingen.de.
H Ekkehard NeuhausPlant Physiology, Technical University Kaiserslautern, 67663, Kaiserslautern, Germany. neuhaus@rhrk.uni-kl.de.
Richard ZimmermannMedical Biochemistry and Molecular Biology, Saarland University, 66421, Homburg, Germany. richard.zimmermann@uks.eu.
Sven LangMedical Biochemistry and Molecular Biology, Saarland University, 66421, Homburg, Germany.
Ilka HaferkampPlant Physiology, Technical University Kaiserslautern, 67663, Kaiserslautern, Germany.
Saarland University · DEUniversity of Kaiserslautern · DEUniversity of Göttingen · DE

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) BO3643/3-2Deutsche Forschungsgemeinschaft (German Research Foundation) IRTG 1830Deutsche Forschungsgemeinschaft (German Research Foundation) IRTG1830Deutsche Forschungsgemeinschaft (German Research Foundation) SFB 1027Deutsche Forschungsgemeinschaft (German Research Foundation) SFB 1190Deutsche Forschungsgemeinschaft (German Research Foundation) SFB 894
6 · The paper itself

Abstract

To fulfill its role in protein biogenesis, the endoplasmic reticulum (ER) depends on the Hsp70-type molecular chaperone BiP, which requires a constant ATP supply. However, the carrier that catalyzes ATP uptake into the ER was unknown. Here, we report that our screen of gene expression datasets for member(s) of the family of solute carriers that are co-expressed with BiP and are ER membrane proteins identifies SLC35B1 as a potential candidate. Heterologous expression of SLC35B1 in E. coli reveals that SLC35B1 is highly specific for ATP and ADP and acts in antiport mode. Moreover, depletion of SLC35B1 from HeLa cells reduces ER ATP levels and, as a consequence, BiP activity. Thus, human SLC35B1 may provide ATP to the ER and was named AXER (ATP/ADP exchanger in the ER membrane). Furthermore, we propose an ER to cytosol low energy response regulatory axis (termed lowER) that appears as central for maintaining ER ATP supply.

Indexed as

Adenosine DiphosphateAdenosine TriphosphateAmino Acid SequenceBiological TransportCytosolElectrophoresis, Polyacrylamide GelEndoplasmic ReticulumHeLa CellsHumansMembrane ProteinsMitochondrial MembranesMolecular Sequence DataMonosaccharide Transport ProteinsReal-Time Polymerase Chain ReactionSequence Homology, Amino AcidUDP-Galactose TranslocatorsAdenosine DiphosphateAdenosine TriphosphateMembrane ProteinsMonosaccharide Transport ProteinsUDP-Galactose Translocators

Identifiers

PMID30154480
PMCPMC6113206
OpenAlexW2888117601

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.